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Journal of Bacteriology, July 2007, p. 4749-4755, Vol. 189, No. 13
0021-9193/07/$08.00+0 doi:10.1128/JB.00392-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Department of Physics and Atmospheric Science, Dalhousie University, Halifax, Nova Scotia, Canada, B3H 3J5
Received 15 March 2007/ Accepted 20 April 2007
Phage
lyses the host Escherichia coli at a precisely scheduled time after induction. Lysis timing is determined by the action of phage holins, which are small proteins that induce hole formation in the bacterium's cytoplasmic membrane. We present a two-stage nucleation model of lysis timing, with the nucleation of condensed holin rafts on the inner membrane followed by the nucleation of a hole within those rafts. The nucleation of holin rafts accounts for most of the delay of lysis after induction. Our simulations of this model recover the accurate lysis timing seen experimentally and show that the timing accuracy is optimal. An enhanced holin-holin interaction is needed in our model to recover experimental lysis delays after the application of membrane poison, and such early triggering of lysis is possible only after the inner membrane is supersaturated with holin. Antiholin reduces the delay between membrane depolarization and lysis and leads to an earlier time after which triggered lysis is possible.
Published ahead of print on 27 April 2007.
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